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Cyclase‐associated proteins: CAPacity for linking signal transduction and actin polymerization
Author(s) -
Hubberstey Andrew V.,
Mottillo Emilio P.
Publication year - 2002
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.01-0659rev
Subject(s) - microbiology and biotechnology , actin remodeling , biology , actin binding protein , adenylyl cyclase , actin cytoskeleton , signal transduction , actin , cytoskeleton , biochemistry , cell
Many extracellular signals elicit changes in the actin cytoskeleton, which are mediated through an array of signaling proteins and pathways. One family of proteins that plays a role in regulating actin remodeling in response to cellular signals are the cyclase‐associated proteins (CAPs). CAPs are highly conserved monomeric actin binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. The original CAP was isolated as a component of the Saccharomyces cerevisiae adenylyl cyclase complex that serves as an effector of Ras during nutritional signaling. CAPs are multifunctional molecules that contain domains involved in actin binding, adenylyl cyclase association in yeast, SH3 binding, and oligomerization. Genetic studies in yeast have implicated CAPs in vesicle trafficking and endocytosis. CAPs play a developmental role in multicellular organisms, and studies of Drosophila have illuminated the importance of the actin cytoskeleton during eye development and in establishing oocyte polarity. This review will highlight the critical structural and functional domains of CAPs, describe recent studies that have implied important roles for these proteins in linking cell signaling with actin polymerization, and highlight their roles in vesicle trafficking and development.—Hubberstey, A. V., Mottillo, E. P. Cyclase‐associated proteins: CAPacity for linking signal transduction and actin polymerization. FASEB J. 16, 487–499 (2002)

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